1995
DOI: 10.1016/s0966-842x(00)88879-4
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The defensive role of nonspecific lipid-transfer proteins in plants

Abstract: Plant nonspecific lipid-transfer proteins stimulate the transfer of a broad range of lipids between membranes in vitro. In view of their ability to inhibit bacterial and fungal pathogens, their distribution at high concentrations over exposed surfaces and in the vascular system, and the response of Ltp-gene expression to infection with pathogens, they are now thought to be active plant-defense proteins.

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Cited by 329 publications
(201 citation statements)
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“…All plant LTPs tested, including those from barley and maize, have antimicrobial activity although the relative activities of different LTPs vary between organisms (Garcia- Olmedo et al, 1995). This pathogen defence role is consistent with the in vivo location of the proteins.…”
Section: Functional Significancementioning
confidence: 70%
“…All plant LTPs tested, including those from barley and maize, have antimicrobial activity although the relative activities of different LTPs vary between organisms (Garcia- Olmedo et al, 1995). This pathogen defence role is consistent with the in vivo location of the proteins.…”
Section: Functional Significancementioning
confidence: 70%
“…The antimicrobial action of nsLTPs has also been demonstrated in vitro and in vivo (Cammue et al, 1995). Also, fungal (Garcia-Olmedo et al, 1995) and viral infection (Sohal et al, 1999) induces the expression of nsLTP genes. Such an antipathogenic role could also be envisaged in potato, particularly as it is known that potato produces a range of different prophylactic defense proteins in tubers.…”
Section: Discussionmentioning
confidence: 99%
“…Little information concerning possible mecha-*Corresponding author. Fax (34) (4) 464-8500 nisms of action are available for the more recently described plant peptide families, such as the so-called lipid transfer proteins (LTP), which are extracellular peptides involved in plant defense against pathogens [10][11][12], and the DL1 and DL2 families of antipathogenic peptides, which may be phylogenetically related to each other and share some common features with snake-venom desintegrins [ [13], M. Moreno et al, in preparation]. From the structural point of view, LTP2 from barley is known to contain 90 amino acid residues, with a positive charge/mass ratio of 0.9 X 10~3 [10], while no equivalent data are available for the DL1 and DL2 peptides.…”
Section: Introductionmentioning
confidence: 99%